PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20226094-1 2010 BACKGROUND: Myosin performs ATP free energy transduction into mechanical work in the motor domain of the myosin heavy chain (MHC). Adenosine Triphosphate 28-31 major histocompatibility complex, class I, C Homo sapiens 105-123 20226094-1 2010 BACKGROUND: Myosin performs ATP free energy transduction into mechanical work in the motor domain of the myosin heavy chain (MHC). Adenosine Triphosphate 28-31 major histocompatibility complex, class I, C Homo sapiens 125-128 17475667-5 2007 Isoform differences located in the S1 head region of the MHC can alter actin binding and rates of ATP hydrolysis. Adenosine Triphosphate 98-101 major histocompatibility complex, class I, C Homo sapiens 57-60 11181631-3 2001 Because the myosin heavy chain (MHC) is the site of ATP hydrolysis and actin binding, we focus on the mechanical and energetic properties of different MHC isoforms. Adenosine Triphosphate 52-55 major histocompatibility complex, class I, C Homo sapiens 12-30 15621050-8 2005 Significant linear correlations were found between MHC isoform composition, ATP consumption and rate of force redevelopment. Adenosine Triphosphate 76-79 major histocompatibility complex, class I, C Homo sapiens 51-54 14563688-2 2003 The expression of MHC-B, which contains an insert at the ATP binding pocket, has been linked to enhanced contractile kinetics. Adenosine Triphosphate 57-60 major histocompatibility complex, class I, C Homo sapiens 18-21 11714757-4 2001 Unlike clustering of HLA-C at the immune synapse, intercellular transfer of HLA-C is dependent on NK cell ATP, but not target cell ATP. Adenosine Triphosphate 106-109 major histocompatibility complex, class I, C Homo sapiens 76-81 11181631-3 2001 Because the myosin heavy chain (MHC) is the site of ATP hydrolysis and actin binding, we focus on the mechanical and energetic properties of different MHC isoforms. Adenosine Triphosphate 52-55 major histocompatibility complex, class I, C Homo sapiens 32-35 10573776-9 1999 Almost 100% of the MHC mRNA in the dome, mid bladder body, and base contains a 7-amino acid insert near the ATP-binding region, whereas the MHC in the urethral smooth muscle is only 81% inserted. Adenosine Triphosphate 108-111 major histocompatibility complex, class I, C Homo sapiens 19-22 10494800-2 1999 The myosin heavy chain (MHC) contains the actin- and ATP-binding sites and represents the molecular motor of muscle contraction. Adenosine Triphosphate 53-56 major histocompatibility complex, class I, C Homo sapiens 4-22 10494800-2 1999 The myosin heavy chain (MHC) contains the actin- and ATP-binding sites and represents the molecular motor of muscle contraction. Adenosine Triphosphate 53-56 major histocompatibility complex, class I, C Homo sapiens 24-27 11160066-2 2001 We hypothesized that the reserve capacity for ATP consumption [1 -- (ratio of ATP(iso) to V(max) ATPase)] varies across VL muscle fibers expressing different MHC isoforms. Adenosine Triphosphate 46-49 major histocompatibility complex, class I, C Homo sapiens 158-161 11160066-2 2001 We hypothesized that the reserve capacity for ATP consumption [1 -- (ratio of ATP(iso) to V(max) ATPase)] varies across VL muscle fibers expressing different MHC isoforms. Adenosine Triphosphate 78-81 major histocompatibility complex, class I, C Homo sapiens 158-161 11160066-6 2001 The reserve capacity for ATP consumption was lower for fibers coexpressing MHC(2X) and MHC(2A) compared with fibers singularly expressing MHC(2A) and MHC(slow) (39 vs. 52 and 56%, respectively). Adenosine Triphosphate 25-28 major histocompatibility complex, class I, C Homo sapiens 75-78 11160066-6 2001 The reserve capacity for ATP consumption was lower for fibers coexpressing MHC(2X) and MHC(2A) compared with fibers singularly expressing MHC(2A) and MHC(slow) (39 vs. 52 and 56%, respectively). Adenosine Triphosphate 25-28 major histocompatibility complex, class I, C Homo sapiens 87-90 11160066-6 2001 The reserve capacity for ATP consumption was lower for fibers coexpressing MHC(2X) and MHC(2A) compared with fibers singularly expressing MHC(2A) and MHC(slow) (39 vs. 52 and 56%, respectively). Adenosine Triphosphate 25-28 major histocompatibility complex, class I, C Homo sapiens 87-90 11160066-6 2001 The reserve capacity for ATP consumption was lower for fibers coexpressing MHC(2X) and MHC(2A) compared with fibers singularly expressing MHC(2A) and MHC(slow) (39 vs. 52 and 56%, respectively). Adenosine Triphosphate 25-28 major histocompatibility complex, class I, C Homo sapiens 87-90 11343969-6 2000 Four of the suppressors identified to date reside in the MhC head, around the actin-binding site and near the lips of the pocket where ATP is hydrolyzed. Adenosine Triphosphate 135-138 major histocompatibility complex, class I, C Homo sapiens 57-60 10468663-9 1999 Single fibre studies have demonstrated a relationship between ATP phosphorylation potential and MHC isoform complement. Adenosine Triphosphate 62-65 major histocompatibility complex, class I, C Homo sapiens 96-99 9038850-3 1997 We determined to what extent the synthesis rate of mixed muscle protein in humans reflects that of myosin heavy chain (MHC), the main contractile protein responsible for the conversion of ATP to mechanical energy as muscle contraction. Adenosine Triphosphate 188-191 major histocompatibility complex, class I, C Homo sapiens 99-117 9730972-7 1998 A nucleotide binding site, which is located at residues 660-674, controls binding of AMPD1 to MHC in response to changes in intracellular ATP concentration. Adenosine Triphosphate 138-141 major histocompatibility complex, class I, C Homo sapiens 94-97 9730972-8 1998 Deletion analyses demonstrate that the amino-terminal 65 residues of AMPD1 play a critical role in modulating the sensitivity to ATP-induced inhibition of MHC binding. Adenosine Triphosphate 129-132 major histocompatibility complex, class I, C Homo sapiens 155-158 9730972-9 1998 Alternative splicing of the AMPD1 gene product, which alters the sequence of residues 8-12, produces two AMPD1 isoforms that exhibit different MHC binding properties in the presence of ATP. Adenosine Triphosphate 185-188 major histocompatibility complex, class I, C Homo sapiens 143-146 9038850-3 1997 We determined to what extent the synthesis rate of mixed muscle protein in humans reflects that of myosin heavy chain (MHC), the main contractile protein responsible for the conversion of ATP to mechanical energy as muscle contraction. Adenosine Triphosphate 188-191 major histocompatibility complex, class I, C Homo sapiens 119-122 32997515-5 2020 ATP turnover of SRX is faster in MHC IIAX fibers compared to MHC I and IIA fibers (p = 0.001). Adenosine Triphosphate 0-3 major histocompatibility complex, class I, C Homo sapiens 33-36 8320827-2 1993 Amino acid sequence comparison of the human cardiac alpha- and beta-MHC have demonstrated that there are, at least, 7 isoform-specific divergent regions, including important binding protein-related sites such as ATP, actin and myosin light chain. Adenosine Triphosphate 212-215 major histocompatibility complex, class I, C Homo sapiens 68-71 1569576-6 1992 The sequence of this neuronal MHC is compared with those of other non-muscle MHCs, to which it shows an overall similarity of structure, especially with respect to conserved regions within the head (ATP binding site, actin binding site, reactive thiols) and the presence of an alpha-helical coiled-coil tail that can be arranged as 28-residue repeating units plus four skip residues. Adenosine Triphosphate 199-202 major histocompatibility complex, class I, C Homo sapiens 30-33 27942960-8 2016 The ATP study demonstrated that, in beta-MHC containing fibers, K 1 (ATP association constant) was greater (1.7x), k 2 and k -2 (cross-bridge detachment and its reversal rate constants) were smaller (x0.6). Adenosine Triphosphate 4-7 major histocompatibility complex, class I, C Homo sapiens 41-44 27942960-8 2016 The ATP study demonstrated that, in beta-MHC containing fibers, K 1 (ATP association constant) was greater (1.7x), k 2 and k -2 (cross-bridge detachment and its reversal rate constants) were smaller (x0.6). Adenosine Triphosphate 69-72 major histocompatibility complex, class I, C Homo sapiens 41-44